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Metalloproteins as Studied by Electron Paramagnetic Resonance

  • J. Peisach
  • W. E. Blumberg

Abstract

Low-temperature EPR spectroscopy has been used to study copper- and iron-containing proteins. The information derived from these studies includes the oxido-reduction function of the metal, special features of the ligand field of the metal especially as they pertain to the protein environment, and interactions between paramagnetic centers. Correlations which exist between spectrophotometric and magnetic properties are related to the spin states of paramagnetic species. These are used to describe spin exchange phenomena in such systems as oxyhemoglobin, oxyhemocyanin, cytochrome c oxidase, copper uroporphyrin, and various model metal complexes.

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Copyright information

© Plenum Press, New York 1969

Authors and Affiliations

  • J. Peisach
    • 1
  • W. E. Blumberg
    • 2
  1. 1.Departments of Pharmacology and Molecular Biology Albert Einstein College of MedicineYeshiva UniversityNew YorkUSA
  2. 2.Bell Telephone LaboratoriesMurray HillUSA

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